ID   SBCC_STAAW              Reviewed;        1009 AA.
AC   Q8NWV1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Nuclease SbcCD subunit C;
GN   Name=sbcC; OrderedLocusNames=MW1233;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: SbcCD cleaves DNA hairpin structures. These structures can
CC       inhibit DNA replication and are intermediates in certain DNA
CC       recombination reactions. The complex acts as a 3'->5' double strand
CC       exonuclease that can open hairpins. It also has a 5' single-strand
CC       endonuclease activity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of SbcC and SbcD. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SMC family. SbcC subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000033; BAB95098.1; -; Genomic_DNA.
DR   RefSeq; WP_000803157.1; NC_003923.1.
DR   AlphaFoldDB; Q8NWV1; -.
DR   SMR; Q8NWV1; -.
DR   KEGG; sam:MW1233; -.
DR   HOGENOM; CLU_004785_2_1_9; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   CDD; cd03279; ABC_sbcCD; 1.
DR   Gene3D; 1.10.287.510; Helix hairpin bin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
DR   NCBIfam; NF041751; sbcc_Staph; 1.
DR   PANTHER; PTHR32114; ABC TRANSPORTER ABCH.3; 1.
DR   PANTHER; PTHR32114:SF2; ABC TRANSPORTER ABCH.3; 1.
DR   Pfam; PF13476; AAA_23; 1.
DR   Pfam; PF13558; SbcC_Walker_B; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; DNA recombination; DNA replication; Endonuclease;
KW   Exonuclease; Hydrolase; Nuclease; Nucleotide-binding.
FT   CHAIN           1..1009
FT                   /note="Nuclease SbcCD subunit C"
FT                   /id="PRO_0000338468"
FT   COILED          176..364
FT                   /evidence="ECO:0000255"
FT   COILED          392..502
FT                   /evidence="ECO:0000255"
FT   COILED          535..802
FT                   /evidence="ECO:0000255"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1009 AA;  117318 MW;  EA310258D258E5EB CRC64;
     MKPLHLKLNN FGPFLKEEID FSKIDNNELF LISGKTGSGK TMIFDAMTYA LFGKASTEQR
     EENDLRSHFA DGKQPMSVTF EFQLNHRIYK VHRQGPYIKE GNTTKTNAKF DVFEMVDGKY
     EIRESKVISG TQFIIELLGV NADQFRQLFI LPQGEFKRFL ISNSREKQGI LRTLFDSEKF
     EAIREILKEE VKKEKAQIEN RYQQIDLLWQ EIESFDDDNI KGLLEVATQQ IDKLIENIPL
     LQARSKEILA SVNESKETAI KEFEIIEKKT LENNILKDNI NQLNKNKIDF VQLKEQQPEI
     EGIEAKLKLL QDITNLLNYI ENREKIETKI ANSKKDISKT NNKILNLDCD KRNIDKEKKM
     LEENGDLIES KISFIDKTRV LFNDINKYQQ SYLNIERLRT EGEQLGDELN DLIKGLETVE
     DSIGNNESDY EKIIELNNTI TNINNEINII KENEKAKAEL DKLLGSKQEL ENQINEETSI
     LKNLEIKLDR YDKTKLDLND KESFISEIKS AVNIGDQCPI CGNEIQDLGH HIDFDSIAKR
     QNEIKEIEAN IHAIKSNIAV HNSEIKFVNE KISNINIKTQ SDFSLEVLNK RLLENENALN
     NQRDLNKFIE QMKEEKDNLT LQIHNKQLRL NKNESELKLC RDLITEFETL SKYNNITNFE
     VDYKKYVQDV NQHQELSKEI EDKLMQLSQR KLIEQNNLNH YENQLETYNN DLELNEQSIE
     MEMSRLNLTD DNDIDEIIAW RGEQEELEQK RDTYKKRYHE FEMEIARLES LTKDKELLDS
     DKLKDEYELK KGKMNTLIDE YSAVHYQCQN NINKTQSIVS HINYLNQELK DQQEIFQLAE
     IVSGKNNKNL TLENFVLIYY LDQIIAQANL RLATMSDNRY QLIRREAVSH GLSGLEIDVF
     DLHSNKSRHI SSLSGGETFQ SSLALALGLS EIVQQQSGGI SLESIFIDEG FGTLDQETLE
     TALDTLLNLK STGRMVGIIS HVSELKNRIP LVLEVKSDQY QSSTRFKRN
//